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A more recent version of this article appeared on November 1, 2005
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Submitted on April 3, 2005
Revised on August 12, 2005
Accepted on August 16, 2005
*Max-Planck-Institut für Terrestrische Mikrobiologie, Karl-von-Frisch-Straße, D-35043 Marburg, Germany;
Eckhard Thines, Institut für Biotechnologie und Wirkstoff-Forschung, TU Kaiserslautern, D-67663 Kaiserslautern, Germany;
Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany
Monitoring Editor: David Drubin
Long-distance transport is crucial for polar growing cells, such as neurons and fungal hyphae. Kinesins and myosins participate in this, but their functional interplay is poorly understood. Here we investigate the role of kinesin motors in hyphal growth of the plant pathogen Ustilago maydis. Although the microtubule plus-ends are directed to the hyphal tip, out of all 10 kinesins analyzed, only conventional kinesin (Kinesin-1), and Unc104/Kif1A-like kinesin (Kinesin-3) were up-regulated in hyphae and are essential for extended hyphal growth.
kin1 and
kin3 mutant hyphae grew irregular and remained short, but were still able to grow polarized. No additional phenotype was detected in
kin1rkin3 double mutants, but polarity was lost in
myo5rkin1 and
myo5rkin3 mutant cells, suggesting that kinesins and class V myosin cooperate in hyphal growth. Consistent with such a role in secretion, fusion proteins of GFP and Kinesin-1, Myosin-V and Kinesin-3 accumulate in the apex of hyphae, a region where secretory vesicles cluster to form the fungal Spitzenkörper. Quantitative assays revealed a role of Kin3 in secretion of acid phosphatase, whereas Kin1 was not involved. Our data demonstrate that just two kinesins and at least one myosin support hyphal growth.
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